PDBe 4y18

X-ray diffraction
3.5Å resolution

Structure of BRCA1 BRCT domains in complex with Abraxas double phosphorylated peptide

Released:

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Breast cancer type 1 susceptibility protein Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 224 amino acids
Theoretical weight: 25.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P38398 (Residues: 1646-1859; Coverage: 12%)
Gene names: BRCA1, RNF53
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain
BRCA1-A complex subunit Abraxas 1 Chains: I, J, K, L, M, N, O, P
Molecule details ›
Chains: I, J, K, L, M, N, O, P
Length: 11 amino acids
Theoretical weight: 1.41 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q6UWZ7 (Residues: 399-409; Coverage: 3%)
Gene names: ABRA1, ABRAXAS1, CCDC98, FAM175A, UNQ496/PRO1013

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 86.819Å b: 183.726Å c: 190.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.233 0.298
Expression systems:
  • Escherichia coli
  • Not provided